Results 21 to 30 of about 26,505 (243)
The SQSTM1/p62 UBA domain regulates Ajuba localisation, degradation and NF-κB signalling function
PLoS ONE, 2021 The LIM-domain containing protein Ajuba and the scaffold protein SQSTM1/p62 regulate signalling of NF-κB, a transcription factor involved in osteoclast differentiation and survival.
Melanie A. Sultana +8 more
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Considering the mechanism by which droplets of ALS-FTD-associated SQSTM1/p62 mutants cause pathology
Autophagy Reports, 2022 Large numbers of point mutations in SQSTM1/p62 have been identified in amyotrophic lateral sclerosis (ALS) and frontotemporal degeneration (FTD). SQSTM1 interacts with ubiquitinated proteins, undergoing liquid-liquid phase separation, and the resulting ...
Yoshinobu Ichimura, Masaaki Komatsu
doaj +1 more source
Virulence, 2022 DNA damage-inducible transcript 3 (DDIT3), a transcription factor, is typically involved in virus replication control. We are the first to report that DDIT3 promotes the replication of bovine viral diarrhea virus, an RNA virus, by inhibiting innate ...
Song Wang +8 more
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SQSTM1-mediated clearance of cytoplasmic mutant TARDBP/TDP-43 in the monkey brain
, 2021 The cytoplasmic accumulation and aggregates of TARDBP/TDP-43 (TAR DNA binding protein) are a pathological hallmark in amyotrophic lateral sclerosis and frontotemporal lobar degeneration. We previously reported that the primate specific cleavage of TARDBP
Jianmeng Ye (11868459) +13 more
core +1 more source
Frameshift mutation in SQSTM1 causes proximal myopathy with rimmed vacuoles: A case report
Frontiers in Neurology, 2023 p62/Sequestosome-1 (SQSTM1) is a stress-inducible scaffold protein involved in multiple cellular processes, including apoptosis, inflammation, cell survival, and selective autophagy.
Rui Wu +5 more
doaj +1 more source
Interaction of SQSTM1 with the motor protein dynein: SQSTM1 is required for normal dynein function and trafficking [PDF]
Journal of Cell Science, 2014 The dynein motor protein complex is required for retrograde transport of vesicular cargo and for transport of aggregated proteins along microtubules for processing and degradation at perinuclear aggresomes. Disruption of this process leads to dysfunctional endosome accumulation and increased protein aggregation in the cell cytoplasm, both pathological ...
Luis, Calderilla-Barbosa +7 more
openaire +2 more sources
Mechanistic insight into the regulation of SQSTM1/p62 [PDF]
Autophagy, 2019 SQSTM1/p62 facilitates responses to various cellular stresses and has been implicated in human diseases. This protein functions as a major cytoplasmic signaling hub and has multiple binding partners, including arginylated (Nt-R) proteins that are recognized by the ZZ domain of SQSTM1/p62 (SQSTM1/p62ZZ).
Yi Zhang +7 more
openaire +2 more sources
Cellular & Molecular Biology Letters, 2023 Background Ubiquitin–proteasome-system-mediated clearance of misfolded proteins is essential for cells to maintain proteostasis and reduce the proteotoxicity caused by these aberrant proteins.
Chenliang Zhang +3 more
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Viruses, 2021 Selective autophagy mediates the degradation of cytoplasmic cargos, such as damaged organelles, invading pathogens, and protein aggregates. However, whether it targets double-stranded RNA (dsRNA) of intracellular pathogens is still largely unknown. Here,
Chenyang Xu +5 more
doaj +1 more source
PLoS ONE, 2020 The NUP98 and NUP214 nucleoporins (NUPs) are recurrently fused to heterologous proteins in leukemia. The resulting chimeric oncoproteins retain the phenylalanine-glycine (FG) repeat motifs of the NUP moiety that mediate interaction with the nuclear ...
Catherine P Lavau +7 more
doaj +1 more source